Category: Lab Notes: Biochemistry

Lysine malonylation is a metabolic post-translational modification that connects malonyl-CoA metabolism with protein function, mitochondrial activity, epigenetic regulation and cellular homeostasis.

Protein deamidation is a chemical modification in which asparagine or glutamine residues are converted into acidic amino acids. Learn how deamidation affects protein structure, stability, aging, proteostasis, disease, and therapeutic proteins.

Protein citrullination is a calcium-dependent post-translational modification that converts arginine into citrulline. Explore PAD enzymes, histone citrullination, NETosis, inflammation, rheumatoid arthritis, autoimmunity, cancer, and citrullination proteomics.

Protein ADP-ribosylation is an important post-translational modification that uses NAD+ to regulate proteins and cellular pathways. Explore mono- and poly-ADP-ribosylation, PARP enzymes, DNA repair, chromatin regulation, cancer, metabolism, inflammation, and cell death.

Protein SUMOylation is an important post-translational modification that regulates protein activity, localization, stability, molecular interactions, gene expression, DNA repair, and cellular stress responses. Learn about SUMO proteins, Ubc9, SUMO ligases, SENPs, SUMO–ubiquitin crosstalk, and SUMO proteomics.

Protein methylation is an important post-translational modification that regulates protein function, chromatin structure, gene expression, signaling, and cellular metabolism. Learn about lysine and arginine methylation, methyltransferases, demethylases, histone methylation, methylproteomics, and disease.

Protein acetylation is an important post-translational modification that regulates protein activity, stability, localization, interactions, gene expression, and metabolism. Learn about lysine acetylation, acetyltransferases, deacetylases, histone acetylation, acetylomics, and the role of acetylation in disease.

Post-translational modifications (PTMs) are biochemical changes that occur during or after protein synthesis and regulate protein structure, activity, stability, localization, interactions, and degradation. This overview introduces the major types of PTMs, their biological functions, mechanisms, role in disease, and methods used to study protein modifications.

Protein folding is the process by which newly synthesized proteins acquire their functional three-dimensional structures. Discover how folding occurs, what influences it, and how cells manage misfolded proteins.

Peptides are short chains of amino acids that act as essential messengers, regulators, and structural molecules in living organisms. This article explores how peptides are formed, how they function, and why they are vital in biology and modern medicine.

Metabolic disorders occur when biochemical pathways responsible for processing nutrients and generating energy become disrupted. These conditions may involve defects in glycolysis, fatty‑acid oxidation, mitochondrial function or endocrine signalling. Their consequences range from mild metabolic imbalance to severe systemic disease, affecting growth, neurological function and long‑term health.

Hydrolytic enzymes catalyse the breakdown of macromolecules by adding water to chemical bonds. Found in lysosomes, digestive organs and immune cells, they degrade proteins, nucleic acids, lipids and carbohydrates. Their activity maintains cellular homeostasis, supports nutrient acquisition and protects against pathogens, while dysregulation contributes to metabolic and degenerative diseases.

The ubiquitin-proteasome system is the master regulator of the cell cycle, controlling cyclin degradation, checkpoint progression, and mitotic exit. This comprehensive guide covers UPS mechanisms in G1/S transition, S phase, mitosis, and cancer therapy.

Protein degradation is a vital cellular process that removes damaged or unnecessary proteins to maintain homeostasis. This article explains the ubiquitin–proteasome system, autophagy, and their roles in cellular regulation and disease.